Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Amidophosphoribosyltransferase

Gene

PPAT

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathway: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Amidophosphoribosyltransferase (GPAT), Amidophosphoribosyltransferase (PPAT), Amidophosphoribosyltransferase (PPAT)
  2. Trifunctional purine biosynthetic protein adenosine-3 (GART)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121NucleophilePROSITE-ProRule annotation
Metal bindingi280 – 2801Iron-sulfur (4Fe-4S)By similarity
Metal bindingi327 – 3271MagnesiumBy similarity
Metal bindingi389 – 3891MagnesiumBy similarity
Metal bindingi390 – 3901MagnesiumBy similarity
Metal bindingi426 – 4261Iron-sulfur (4Fe-4S)By similarity
Metal bindingi496 – 4961Iron-sulfur (4Fe-4S)By similarity
Metal bindingi499 – 4991Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_116007. De novo synthesis of IMP.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Amidophosphoribosyltransferase (EC:2.4.2.14)
Short name:
ATase
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name:
GPAT
Gene namesi
Name:PPAT
Synonyms:GPAT
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1111CuratedPRO_0000029281Add
BLAST
Chaini12 – 510499AmidophosphoribosyltransferasePRO_0000029282Add
BLAST

Proteomic databases

PaxDbiP28173.
PRIDEiP28173.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9031.ENSGALP00000022273.

Structurei

3D structure databases

ProteinModelPortaliP28173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 261250Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0034.
HOGENOMiHOG000033688.
HOVERGENiHBG002589.
InParanoidiP28173.
KOiK00764.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00310. GATase_2. 2 hits.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELEELGIRE ECGVFGCIAA GVWPTELDVP HVITLGLVGL QHRGQESAGI
60 70 80 90 100
VTSDGESSQA FKVHKGMGLI NHVFNADSLK KLYVSNLGIG HTRYSTSGIS
110 120 130 140 150
ELQNCQPFVV ETLHGKIAVA HNGELTNAVR LRRKLMRHGV GLSTSSDSEL
160 170 180 190 200
ITQLLAFTPP LENDDTADWV ARIKNLMNET PTSYSLLIMH KDIIYAVRDP
210 220 230 240 250
YGNRPLCIGR LIPVGDINGK GKDNSETEGW VVSSESCSFL SIGAEYYREV
260 270 280 290 300
LPGEIVKISR YDVQTLDVVP RPEGDPSAFC IFEYVYFARP DSIFEGQMVY
310 320 330 340 350
SVRRRCGQQL AIEAPVEADL VSTVPESATP AALGYAQKCG LPYVEVLCKN
360 370 380 390 400
RYVGRTFIQP NMRLRQLGVA KKFGVLSDNF KGKRVVIIDD SIVRGNTISP
410 420 430 440 450
IIKLLRESGA KEVHIRVASP PIRFPCYMGI NIPTKEELIA NRPEFHDLAN
460 470 480 490 500
YIGADSVVYL SVEGLVSSVQ ESIKARKENE NSLKTQKSRV GKIGHCTACL
510
TGDYPVELEW
Length:510
Mass (Da):56,257
Last modified:December 1, 1992 - v1
Checksum:iF4371FE1FEC7C744
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60069 mRNA. Translation: AAA62736.1.
L12533 Unassigned DNA. Translation: AAA17895.1.
PIRiA38337.
RefSeqiNP_001004401.1. NM_001004401.1.
UniGeneiGga.2870.

Genome annotation databases

GeneIDi422743.
KEGGigga:422743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60069 mRNA. Translation: AAA62736.1.
L12533 Unassigned DNA. Translation: AAA17895.1.
PIRiA38337.
RefSeqiNP_001004401.1. NM_001004401.1.
UniGeneiGga.2870.

3D structure databases

ProteinModelPortaliP28173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000022273.

Protein family/group databases

MEROPSiC44.001.

Proteomic databases

PaxDbiP28173.
PRIDEiP28173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi422743.
KEGGigga:422743.

Organism-specific databases

CTDi5471.

Phylogenomic databases

eggNOGiCOG0034.
HOGENOMiHOG000033688.
HOVERGENiHBG002589.
InParanoidiP28173.
KOiK00764.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
ReactomeiREACT_116007. De novo synthesis of IMP.

Miscellaneous databases

NextBioi20825333.
PROiP28173.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00310. GATase_2. 2 hits.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of avian glutamine phosphoribosylpyrophosphate amidotransferase. Conservation of a bacterial propeptide sequence supports a role for posttranslational processing."
    Zhou G., Dixon J.E., Zalkin H.
    J. Biol. Chem. 265:21152-21159(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Coexpression of two closely linked avian genes for purine nucleotide synthesis from a bidirectional promoter."
    Gavalas A., Dixon J.E., Brayton K.A., Zalkin H.
    Mol. Cell. Biol. 13:4784-4792(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-42.
  3. Erratum
    Gavalas A., Dixon J.E., Brayton K.A., Zalkin H.
    Mol. Cell. Biol. 13:7977-7977(1993)

Entry informationi

Entry nameiPUR1_CHICK
AccessioniPrimary (citable) accession number: P28173
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 24, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.